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Papain is a protease that consists of α-helical and β-sheet domains which   unfold almost independently. Both, papain considerable thermal stability and   sodium dodecyl sulphate (SDS) resistance have been shown. However, the   ability of each domain to unfold upon thermal and SDS denaturation has never   been studied. This work shows that fruit papain has slightly higher thermal   inactivation resistance when it is compared to stem papain with rather high   activation energy (Ea) of 223 ± 16 kJmol-1 and Tm50 value of 79 ± 2 °C. SDS   resistance of fruit papain was estimated by SDS-PAGE analysis and activity   staining. It has been noted that, in the presence of SDS, unless heat energy   was applied in order to unfold papain, the protein remained active.   Furthermore, it has been proven via Fourier transform infrared spectroscopy   (FT-IR) that α-helical domain of fruit papain is more prone to unfolding at   elevated temperatures and in the presence of SDS then β-sheet rich domain.   Thermal denaturation of papain without detergent present led to accelerated   formation of aggregation specific intermolecular β-sheets as compared to   native protein. Presented results are both, of fundamental and application   importance. [Projekat Ministarstva nauke Republike Srbije, br. 172049

Evidence of β-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulphate denaturation